Abstract
Penicillin G acylase (PGA) has been immobilized on a lanthanum‐incorporated mesostructured cellular foam (La‐MCF) support by using the interaction between the strong Lewis acid sites on the surface of La‐MCF and the free amino groups of lysine residues of PGA. The La‐MCF support was successfully synthesized in situ through the addition of a citric acid (CA) complexant. The results of pyridine‐IR spectroscopy show the presence of strong Lewis acid sites on the surface of the prepared La‐MCF (with CA), attributed to the incorporation of lanthanum species into the framework of MCF. Through interaction with the strong Lewis acid sites, the enzymes can be firmly immobilized on the surface of the support. The results indicate that PGA/La‐MCF (with CA) exhibits a high specific activity and greatly enhanced operational stability. For the hydrolysis of penicillin G potassium salt, the initial specific activity of PGA/La‐MCF (with CA) reaches 10023 U/g. Even after being recycled 10 times, PGA/La‐MCF (with CA) retains 89 % of its initial specific activity, much higher than the 77 % of PGA/Si‐MCF.
